Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Mechanism of Cu(A) assembly.

Literature DB >> 18758441

Mechanism of Cu(A) assembly.

Luciano A Abriata¹, Lucia Banci, Ivano Bertini, Simone Ciofi-Baffoni, Petros Gkazonis, Georgios A Spyroulias, Alejandro J Vila, Shenlin Wang.

Abstract

Copper is essential for proper functioning of cytochrome c oxidases, and therefore for cellular respiration in eukaryotes and many bacteria. Here we show that a new periplasmic protein (PCu(A)C) selectively inserts Cu(I) ions into subunit II of Thermus thermophilus ba(3) oxidase to generate a native Cu(A) site. The purported metallochaperone Sco1 is unable to deliver copper ions; instead, it works as a thiol-disulfide reductase to maintain the correct oxidation state of the Cu(A) cysteine ligands.

Entities: Chemical Disease Gene Mutation Species

Mesh：

Substances：

Year: 2008 PMID： 18758441 PMCID： PMC2596924 DOI： 10.1038/nchembio.110

Source DB: PubMed Journal: Nat Chem Biol ISSN： 1552-4450 Impact factor: 15.040

21 in total

Review 1. Copper trafficking to the mitochondrion and assembly of copper metalloenzymes.

Authors: Paul A Cobine; Fabien Pierrel; Dennis R Winge
Journal: Biochim Biophys Acta Date: 2006-03-31

2. Crystal structure of human SCO1: implications for redox signaling by a mitochondrial cytochrome c oxidase "assembly" protein.

Authors: John C Williams; Carolyn Sue; Graham S Banting; Hua Yang; D Moira Glerum; Wayne A Hendrickson; Eric A Schon
Journal: J Biol Chem Date: 2005-01-19 Impact factor: 5.157

3. A copper(I) protein possibly involved in the assembly of CuA center of bacterial cytochrome c oxidase.

Authors: Lucia Banci; Ivano Bertini; Simone Ciofi-Baffoni; Efthalia Katsari; Nikolaos Katsaros; Karel Kubicek; Stefano Mangani
Journal: Proc Natl Acad Sci U S A Date: 2005-03-07 Impact factor: 11.205

4. Characterization of the redox and metal binding activity of BsSco, a protein implicated in the assembly of cytochrome c oxidase.

Authors: Iveta Imriskova-Sosova; Diann Andrews; Katherine Yam; David Davidson; Brahm Yachnin; Bruce C Hill
Journal: Biochemistry Date: 2005-12-27 Impact factor: 3.162

5. Spectroscopic studies of metal binding and metal selectivity in Bacillus subtilis BSco, a Homologue of the Yeast Mitochondrial Protein Sco1p.

Authors: Luisa Andruzzi; Michiko Nakano; Mark J Nilges; Ninian J Blackburn
Journal: J Am Chem Soc Date: 2005-11-30 Impact factor: 15.419

6. A hint for the function of human Sco1 from different structures.

Authors: Lucia Banci; Ivano Bertini; Vito Calderone; Simone Ciofi-Baffoni; Stefano Mangani; Manuele Martinelli; Peep Palumaa; Shenlin Wang
Journal: Proc Natl Acad Sci U S A Date: 2006-05-30 Impact factor: 11.205

7. Crystal structure of yeast Sco1.

Authors: Carnie Abajian; Amy C Rosenzweig
Journal: J Biol Inorg Chem Date: 2006-03-29 Impact factor: 3.358

8. Human Sco1 functional studies and pathological implications of the P174L mutant.

Authors: Lucia Banci; Ivano Bertini; Simone Ciofi-Baffoni; Iliana Leontari; Manuele Martinelli; Peep Palumaa; Rannar Sillard; Shenlin Wang
Journal: Proc Natl Acad Sci U S A Date: 2006-12-20 Impact factor: 11.205

9. The functions of Sco proteins from genome-based analysis.

Authors: Lucia Banci; Ivano Bertini; Gabriele Cavallaro; Antonio Rosato
Journal: J Proteome Res Date: 2007-02-15 Impact factor: 4.466

10. A structural characterization of human SCO2.

Authors: Lucia Banci; Ivano Bertini; Simone Ciofi-Baffoni; Ioannis P Gerothanassis; Iliana Leontari; Manuele Martinelli; Shenlin Wang
Journal: Structure Date: 2007-09 Impact factor: 5.006

53 in total

Review 1. Biogenesis of cbb(3)-type cytochrome c oxidase in Rhodobacter capsulatus.

Authors: Seda Ekici; Grzegorz Pawlik; Eva Lohmeyer; Hans-Georg Koch; Fevzi Daldal
Journal: Biochim Biophys Acta Date: 2011-11-04

2. A novel heme a insertion factor gene cotranscribes with the Thermus thermophilus cytochrome ba3 oxidase locus.

Authors: Carolin Werner; Oliver-Matthias H Richter; Bernd Ludwig
Journal: J Bacteriol Date: 2010-07-09 Impact factor: 3.490

3. Flexibility of the metal-binding region in apo-cupredoxins.

Authors: María-Eugenia Zaballa; Luciano A Abriata; Antonio Donaire; Alejandro J Vila
Journal: Proc Natl Acad Sci U S A Date: 2012-05-29 Impact factor: 11.205

4. The ScoI homologue SenC is a copper binding protein that interacts directly with the cbb₃-type cytochrome oxidase in Rhodobacter capsulatus.

Authors: Eva Lohmeyer; Sebastian Schröder; Grzegorz Pawlik; Petru-Iulian Trasnea; Annette Peters; Fevzi Daldal; Hans-Georg Koch
Journal: Biochim Biophys Acta Date: 2012-07-04

5. Sco proteins are involved in electron transfer processes.

Authors: Lucia Banci; Ivano Bertini; Simone Ciofi-Baffoni; Tatiana Kozyreva; Mirko Mori; Shenlin Wang
Journal: J Biol Inorg Chem Date: 2010-12-23 Impact factor: 3.358

6. Disparate pathways for the biogenesis of cytochrome oxidases in Bradyrhizobium japonicum.

Authors: Doris Bühler; Reinhild Rossmann; Sarah Landolt; Sylvia Balsiger; Hans-Martin Fischer; Hauke Hennecke
Journal: J Biol Chem Date: 2010-03-24 Impact factor: 5.157

Review 7. Response of gram-positive bacteria to copper stress.

Authors: Marc Solioz; Helge K Abicht; Mélanie Mermod; Stefano Mancini
Journal: J Biol Inorg Chem Date: 2009-09-23 Impact factor: 3.358

Review 8. Copper metallochaperones.

Authors: Nigel J Robinson; Dennis R Winge
Journal: Annu Rev Biochem Date: 2010 Impact factor: 23.643

9. Electronic structure of the ground and excited states of the Cu(A) site by NMR spectroscopy.

Authors: Luciano A Abriata; Gabriela N Ledesma; Roberta Pierattelli; Alejandro J Vila
Journal: J Am Chem Soc Date: 2009-02-11 Impact factor: 15.419

10. Analysis of mouse models of cytochrome c oxidase deficiency owing to mutations in Sco2.

Authors: Hua Yang; Sonja Brosel; Rebeca Acin-Perez; Vesna Slavkovich; Ichizo Nishino; Raffay Khan; Ira J Goldberg; Joseph Graziano; Giovanni Manfredi; Eric A Schon
Journal: Hum Mol Genet Date: 2010-01-01 Impact factor: 6.150